PMID: 7117247Jul 1, 1982Paper

A comprehensive approach to the study of collagen primary structure based on high-performance liquid chromatography

European Journal of Biochemistry
M van der Rest, P P Fietzek


A comprehensive approach for the structural microanalysis of collagen based of collagen based on high-performance liquid chromatography (h.p.l.c.) has been developed using calf skin type I collagen as a model system. The alpha, beta and gamma components were separated, after heat denaturation, on a TSK 4000 SW gel permeation column, using a nonvolatile buffer. Monitoring at 210 nm permits the detection of 1 microgram of a single chain. The alpha 1(I) and alpha 2(I) chains were completely resolved using a large-pore reversed-phase column (Vydac 201 TP 4.6) eluted by an aqueous acetonitrile gradient (24-48%) containing 0.01 M heptafluorabutyric acid as an ion-pairing agent. The purified alpha 1(I) chain was digested with CNBr and the resulting fragments separated in the same chromatography system with a gradient containing a 12.8-44.8% acetonitrile gradient. The purified alpha 1(I)CB 3 peptide was further cleaved with trypsin and the resulting peptides separated first by a similar chromatography with a 4-32% acetonitrile gradient. Resolution of some poorly separated peptides was obtained by a rechromatography using trifluoroacetic acid as counterion. The isolated peptides were hydrolyzed and identified by their amino-acid composi...Continue Reading


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